[English] 日本語
Yorodumi
- PDB-7ler: Netrin-1 filament assembly -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 7ler
TitleNetrin-1 filament assembly
ComponentsNetrin-1
KeywordsSIGNALING PROTEIN / heparin binding protein / filament
Function / homology
Function and homology information


regulation of glial cell migration / chemorepulsion of axon / anterior/posterior axon guidance / B cell mediated immunity / Cdc42 protein signal transduction / T cell mediated immunity / motor neuron migration / tissue development / negative regulation of axon extension / substrate-dependent cell migration, cell extension ...regulation of glial cell migration / chemorepulsion of axon / anterior/posterior axon guidance / B cell mediated immunity / Cdc42 protein signal transduction / T cell mediated immunity / motor neuron migration / tissue development / negative regulation of axon extension / substrate-dependent cell migration, cell extension / motor neuron axon guidance / positive regulation of cell motility / nuclear migration / regulation of synapse assembly / inner ear morphogenesis / B cell proliferation / dendrite development / basement membrane / positive regulation of axon extension / glial cell proliferation / positive regulation of glial cell proliferation / substrate adhesion-dependent cell spreading / cytokine activity / cell periphery / animal organ morphogenesis / cell-cell adhesion / actin cytoskeleton / Ras protein signal transduction / extracellular region / nucleoplasm / cytosol
Similarity search - Function
Laminin, N-terminal / Laminin N-terminal (Domain VI) / Laminin N-terminal domain profile. / Laminin N-terminal domain (domain VI) / Laminin-type EGF-like (LE) domain profile. / Laminin-type EGF-like (LE) domain signature. / Laminin-type epidermal growth factor-like domai / Laminin EGF domain / Laminin-type EGF domain / Netrin C-terminal Domain ...Laminin, N-terminal / Laminin N-terminal (Domain VI) / Laminin N-terminal domain profile. / Laminin N-terminal domain (domain VI) / Laminin-type EGF-like (LE) domain profile. / Laminin-type EGF-like (LE) domain signature. / Laminin-type epidermal growth factor-like domai / Laminin EGF domain / Laminin-type EGF domain / Netrin C-terminal Domain / Netrin module, non-TIMP type / UNC-6/NTR/C345C module / Netrin domain / NTR domain profile. / Tissue inhibitor of metalloproteinases-like, OB-fold / EGF-like domain signature 1. / Galactose-binding-like domain superfamily
Similarity search - Domain/homology
Biological speciesGallus gallus (chicken)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 5.99 Å
AuthorsMcDougall, M. / Gupta, M. / Stetefeld, J.
Funding support Canada, 1items
OrganizationGrant numberCountry
Canadian Institutes of Health Research (CIHR)RPA-109759 Canada
CitationJournal: Nat Commun / Year: 2023
Title: The dynamic nature of netrin-1 and the structural basis for glycosaminoglycan fragment-induced filament formation.
Authors: Meier, M. / Gupta, M. / Akgul, S. / McDougall, M. / Imhof, T. / Nikodemus, D. / Reuten, R. / Moya-Torres, A. / To, V. / Ferens, F. / Heide, F. / Padilla-Meier, G.P. / Kukura, P. / Huang, W. ...Authors: Meier, M. / Gupta, M. / Akgul, S. / McDougall, M. / Imhof, T. / Nikodemus, D. / Reuten, R. / Moya-Torres, A. / To, V. / Ferens, F. / Heide, F. / Padilla-Meier, G.P. / Kukura, P. / Huang, W. / Gerisch, B. / Morgelin, M. / Poole, K. / Antebi, A. / Koch, M. / Stetefeld, J.
History
DepositionJan 14, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 23, 2022Provider: repository / Type: Initial release
Revision 1.1Mar 15, 2023Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Aug 16, 2023Group: Data collection / Other
Category: chem_comp_atom / chem_comp_bond / pdbx_database_status
Item: _pdbx_database_status.pdb_format_compatible
Revision 1.3Oct 25, 2023Group: Refinement description / Category: pdbx_initial_refinement_model

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Netrin-1
B: Netrin-1
C: Netrin-1
E: Netrin-1
D: Netrin-1
F: Netrin-1
G: Netrin-1
H: Netrin-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)410,86140
Polymers396,6398
Non-polymers14,22132
Water0
1
A: Netrin-1
B: Netrin-1
C: Netrin-1
E: Netrin-1
D: Netrin-1
F: Netrin-1
G: Netrin-1
H: Netrin-1
hetero molecules
x 6


  • defined by author
  • Evidence: scanning transmission electron microscopy, Negative Stain Electron Microscopy with 2D Alignments
  • 2.47 MDa, 48 polymers
Theoretical massNumber of molelcules
Total (without water)2,465,163240
Polymers2,379,83648
Non-polymers85,327192
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_344-y-2,x-y-1,z-1/31
crystal symmetry operation3_434-x+y-1,-x-2,z-2/31
crystal symmetry operation4_334-x-2,-y-2,z-1/21
crystal symmetry operation5_545y,-x+y-1,z+1/61
crystal symmetry operation6_454x-y-1,x,z-1/61
Unit cell
Length a, b, c (Å)196.690, 196.690, 476.330
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number170
Space group name H-MP65
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 40 through 255 or resid 272...
21(chain B and (resid 40 through 255 or resid 272...
31(chain C and (resid 40 through 255 or resid 272...
41(chain D and (resid 40 through 334 or (resid 335...
51(chain E and (resid 40 through 255 or resid 272...
61(chain F and (resid 40 through 255 or resid 272...
71(chain G and (resid 40 through 255 or resid 272...
81(chain H and (resid 40 through 255 or resid 272...
12chain I
22chain J
32chain K
42chain L
52chain M
62chain N
72chain O
82chain P

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain A and (resid 40 through 255 or resid 272...A40 - 255
121(chain A and (resid 40 through 255 or resid 272...A272 - 334
131(chain A and (resid 40 through 255 or resid 272...A335
141(chain A and (resid 40 through 255 or resid 272...A40 - 457
151(chain A and (resid 40 through 255 or resid 272...A40 - 457
161(chain A and (resid 40 through 255 or resid 272...A40 - 457
171(chain A and (resid 40 through 255 or resid 272...A40 - 457
211(chain B and (resid 40 through 255 or resid 272...B40 - 255
221(chain B and (resid 40 through 255 or resid 272...B272 - 334
231(chain B and (resid 40 through 255 or resid 272...B335
241(chain B and (resid 40 through 255 or resid 272...B40 - 457
251(chain B and (resid 40 through 255 or resid 272...B40 - 457
261(chain B and (resid 40 through 255 or resid 272...B40 - 457
271(chain B and (resid 40 through 255 or resid 272...B40 - 457
311(chain C and (resid 40 through 255 or resid 272...C40 - 255
321(chain C and (resid 40 through 255 or resid 272...C272 - 389
331(chain C and (resid 40 through 255 or resid 272...C390
341(chain C and (resid 40 through 255 or resid 272...C40 - 457
351(chain C and (resid 40 through 255 or resid 272...C40 - 457
361(chain C and (resid 40 through 255 or resid 272...C40 - 457
371(chain C and (resid 40 through 255 or resid 272...C40 - 457
411(chain D and (resid 40 through 334 or (resid 335...D40 - 334
421(chain D and (resid 40 through 334 or (resid 335...D335
431(chain D and (resid 40 through 334 or (resid 335...D40 - 457
441(chain D and (resid 40 through 334 or (resid 335...D40 - 457
451(chain D and (resid 40 through 334 or (resid 335...D40 - 457
461(chain D and (resid 40 through 334 or (resid 335...D40 - 457
511(chain E and (resid 40 through 255 or resid 272...E40 - 255
521(chain E and (resid 40 through 255 or resid 272...E272 - 334
531(chain E and (resid 40 through 255 or resid 272...E335
541(chain E and (resid 40 through 255 or resid 272...E40 - 457
551(chain E and (resid 40 through 255 or resid 272...E40 - 457
561(chain E and (resid 40 through 255 or resid 272...E40 - 457
571(chain E and (resid 40 through 255 or resid 272...E40 - 457
611(chain F and (resid 40 through 255 or resid 272...F40 - 255
621(chain F and (resid 40 through 255 or resid 272...F272 - 334
631(chain F and (resid 40 through 255 or resid 272...F335
641(chain F and (resid 40 through 255 or resid 272...F40 - 457
651(chain F and (resid 40 through 255 or resid 272...F40 - 457
661(chain F and (resid 40 through 255 or resid 272...F40 - 457
671(chain F and (resid 40 through 255 or resid 272...F40 - 457
711(chain G and (resid 40 through 255 or resid 272...G40 - 255
721(chain G and (resid 40 through 255 or resid 272...G272 - 334
731(chain G and (resid 40 through 255 or resid 272...G335
741(chain G and (resid 40 through 255 or resid 272...G40 - 457
751(chain G and (resid 40 through 255 or resid 272...G40 - 457
761(chain G and (resid 40 through 255 or resid 272...G40 - 457
771(chain G and (resid 40 through 255 or resid 272...G40 - 457
811(chain H and (resid 40 through 255 or resid 272...H40 - 255
821(chain H and (resid 40 through 255 or resid 272...H272 - 334
831(chain H and (resid 40 through 255 or resid 272...H335
841(chain H and (resid 40 through 255 or resid 272...H40 - 457
851(chain H and (resid 40 through 255 or resid 272...H40 - 457
861(chain H and (resid 40 through 255 or resid 272...H40 - 457
871(chain H and (resid 40 through 255 or resid 272...H40 - 457
112chain II501 - 531
212chain JJ501 - 531
312chain KK501 - 531
412chain LL501 - 531
512chain MM501 - 531
612chain NN501 - 531
712chain OO501 - 531
812chain PP501 - 531

NCS ensembles :
ID
1
2

-
Components

#1: Protein
Netrin-1 /


Mass: 49579.926 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Gallus gallus (chicken) / Gene: NTN1 / Production host: Homo sapiens (human) / References: UniProt: Q90922
#2: Polysaccharide
alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 910.823 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/3,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3/a4-b1_b4-c1_c3-d1_c6-e1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}LINUCSPDB-CARE
#3: Polysaccharide
2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}LINUCSPDB-CARE
#4: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE / N-Acetylglucosamine


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 16 / Source method: obtained synthetically / Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0
Has ligand of interestN

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 6.71 Å3/Da / Density % sol: 81.66 %
Crystal growTemperature: 293.15 K / Method: vapor diffusion, sitting drop / pH: 8 / Details: 40% MPD, 100 mM Tris

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: CLSI / Beamline: 08B1-1 / Wavelength: 0.97952 Å
DetectorType: RAYONIX MX300HE / Detector: CCD / Date: Sep 12, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97952 Å / Relative weight: 1
Reflection twinOperator: k,h,-l / Fraction: 0.5
ReflectionResolution: 5.99→49.17 Å / Num. obs: 26042 / % possible obs: 99.5 % / Redundancy: 11.1 % / CC1/2: 0.997 / Net I/σ(I): 8
Reflection shellResolution: 5.995→6.208 Å / Num. unique obs: 2565 / CC1/2: 0.777

-
Processing

Software
NameVersionClassification
PHENIX1.18.2-3874_3874refinement
XSCALEdata scaling
XDSdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4OVE
Resolution: 5.99→49.17 Å / Cross valid method: THROUGHOUT / σ(F): 3.44 / Phase error: 38.74 / Stereochemistry target values: TWIN_LSQ_F
RfactorNum. reflection% reflection
Rfree0.3681 1336 5.13 %
Rwork0.3044 24692 -
obs0.3838 26028 99.94 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 1162.7 Å2 / Biso mean: 304.5544 Å2 / Biso min: 102.85 Å2
Refinement stepCycle: final / Resolution: 5.99→49.17 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms25469 0 936 0 26405
Biso mean--290.38 --
Num. residues----3249
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01427044
X-RAY DIFFRACTIONf_angle_d1.08136602
X-RAY DIFFRACTIONf_dihedral_angle_d31.5374126
X-RAY DIFFRACTIONf_chiral_restr0.074054
X-RAY DIFFRACTIONf_plane_restr0.0084746
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A9824X-RAY DIFFRACTION9.809TORSIONAL
12B9824X-RAY DIFFRACTION9.809TORSIONAL
13C9824X-RAY DIFFRACTION9.809TORSIONAL
14D9824X-RAY DIFFRACTION9.809TORSIONAL
15E9824X-RAY DIFFRACTION9.809TORSIONAL
16F9824X-RAY DIFFRACTION9.809TORSIONAL
17G9824X-RAY DIFFRACTION9.809TORSIONAL
18H9824X-RAY DIFFRACTION9.809TORSIONAL
21I528X-RAY DIFFRACTION9.809TORSIONAL
22J528X-RAY DIFFRACTION9.809TORSIONAL
23K528X-RAY DIFFRACTION9.809TORSIONAL
24L528X-RAY DIFFRACTION9.809TORSIONAL
25M528X-RAY DIFFRACTION9.809TORSIONAL
26N528X-RAY DIFFRACTION9.809TORSIONAL
27O528X-RAY DIFFRACTION9.809TORSIONAL
28P528X-RAY DIFFRACTION9.809TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 10

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
5.99-6.210.5111390.50112426256594
6.21-6.460.44941190.45222475259495
6.46-6.750.55321200.44322500262095
6.75-7.10.48331500.44052433258394
7.1-7.550.65161380.48822481261995
7.55-8.130.50871220.42382482260495
8.13-8.940.47981410.41182472261395
8.94-10.230.44361310.35352464259595
10.23-12.840.32141290.30692467259695
12.85-49.170.39581470.34422492263994
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
11.15380.54840.92721.73161.86952.18560.58810.2074-0.9518-0.6091.2850.2011-1.12140.63371.43790.3934-0.79571.0250.96640.64954.2936-112.7383-111.043635.3154
20.1023-0.1202-0.15520.45320.13570.2222-0.6450.1741-0.7911-0.0854-0.23110.63910.4002-0.4946-0.37190.6845-1.08531.290.20020.91983.5462-114.2056-92.198333.0021
30.29670.088-0.63040.22730.2184-0.26710.03790.4466-0.01450.18690.50690.28941.2306-0.0869-0.3916-0.2223-1.23560.2993-1.0307-1.16172.8487-92.4277-97.413726.798
40.57910.46840.21460.64250.18490.146-0.1499-0.41730.3399-0.0606-0.33310.24560.2777-0.5702-0.00980.851-0.74860.3951.6553-0.94982.7269-35.0258-87.968518.6216
50.15730.0449-0.4060.38450.02740.76080.732-0.5620.20080.46920.2861-0.1518-0.4403-0.18531.17561.1390.21731.4445-0.5867-1.41493.4702-51.953-116.5526-1.1358
60.54650.4561-0.08340.5894-0.0880.73160.58860.44470.6229-0.5059-0.15850.47-0.6168-0.4025-0.0197-0.59030.47340.01321.01450.14582.4577-36.8958-111.848-10.5691
70.81930.33840.12780.33450.3356-0.16380.2925-0.4433-0.12540.0368-0.1470.7030.6501-0.39322.08580.3614-0.3596-0.39881.6005-1.86212.2814-36.061-129.8621-7.8223
80.85420.9644-0.38980.96530.05710.2287-0.4080.0233-0.7972-0.1540.4878-0.2432-0.9231-1.03792.9062-0.4084-1.8471-1.0552-1.1018-0.61554.6693-4.0044-163.8826-19.8822
90.62740.2062-0.02030.03230.0560.35820.31890.19230.23890.41950.4249-0.12140.40960.17330.54320.38750.4702-0.49780.65170.96554.1288-134.937-207.9218-7.2712
100.4292-0.05690.35340.3143-0.04430.57670.5795-0.3176-0.13590.28740.2634-0.4280.6189-0.17870.76410.65361.302-0.48590.48280.98944.2681-126.3282-222.17744.0213
110.11740.2183-0.08450.487-0.27110.15130.48530.3504-0.5564-0.8229-0.8559-0.42220.77950.7025-0.00030.18160.8667-0.14421.47830.28183.3456-145.6675-220.7004-10.4415
120.18180.24490.04890.1441-0.070.01710.156-0.1165-0.2593-0.033-0.1805-0.1907-0.55790.1247-0.1809-0.5617-0.1018-0.01392.09451.4192.4985-139.2391-213.4799-3.3891
130.06170.0937-0.13990.115-0.14910.10760.2518-0.4279-0.36180.3626-0.05280.12460.36340.0506-0.3701-0.23190.02612.53980.83011.20852.5969-160.9577-189.7889-16.1923
140.2120.0906-0.15321.0722-0.30050.33960.1475-0.15520.78120.01930.627-0.07120.54850.74951.15751.44290.21161.19110.03810.47032.6015-182.9416-159.9164-20.7015
151.26890.28561.03730.7477-0.0040.93631.14210.163-0.5861-0.49310.6933-0.29120.0339-0.28410.96060.89140.57181.64890.11680.18324.3639-140.9201-128.7041-14.0015
160.1923-0.17770.03320.2633-0.20640.2639-0.1829-0.75970.32430.52-0.3805-0.7133-1.1096-0.46460.2301-0.46580.1424-0.76322.0083-0.5673.1022-156.1787-122.2206-7.8108
170.2558-0.19350.04420.38280.11660.39510.5020.4279-0.24430.2996-0.5806-0.20170.66010.2309-0.43030.0995-0.1389-0.5531.52391.03663.7217-167.2303-146.7379-5.0034
180.8861-0.00460.0430.2532-0.1118-0.1121-0.11210.4962-0.28390.0559-0.01060.1455-0.16850.8628-1.02851.28432.1076-0.72670.20930.18152.6438-199.5013-182.56471.8012
190.1898-0.32380.21360.3941-0.32970.38330.2449-0.0096-0.0565-0.0593-0.0994-0.54760.1158-0.64050.34730.25760.9801-0.9840.33861.09164.2854-121.309-236.9208-53.914
200.488-0.2304-0.28120.51380.08310.16560.0469-0.0004-0.06870.18850.4214-0.42040.56870.5050.17320.99770.6755-0.56092.1891-0.18822.857-123.969-245.2022-55.4823
210.46920.15090.33460.29050.51920.12230.1472-1.09450.3677-0.12110.7907-0.3227-1.00920.7862-0.5897-0.80791.3374-0.0096-0.5465-0.95553.3031-104.4389-252.2106-45.6281
220.0002-0.0016-0.01520.26980.17510.113-0.51950.1586-0.11590.276-0.71190.4992-0.1994-0.8982-0.47520.83370.4511-0.1493-0.4309-1.55223.7649-45.2172-256.5863-37.8082
230.6811-0.35740.08170.7729-0.15860.7620.77890.0313-0.2176-0.34910.68010.35540.18990.35951.3883-0.7831-0.95221.7040.8909-0.4134.0848-76.215-119.9722-56.6039
242.7254-0.18960.16810.3649-0.0268-0.00210.17880.33350.05930.0760.11310.3898-0.01830.4362-0.70461.05661.19760.13432.18031.24513.3978-78.6077-111.8135-51.2258
250.42510.39440.17820.44520.14480.2666-0.05270.3121-0.57130.001-0.1148-0.16280.05320.1045-0.34330.02450.1298-0.17490.7359-0.87112.606-79.6172-97.8656-50.2152
260.0908-0.7112-0.44852.8827-0.19631.04330.95250.4586-0.2940.02250.91571.98010.2147-1.66278.86820.10520.7033-0.09030.33151.17393.1465-114.584-106.1345-42.9008
271.05170.34760.11320.2293-0.07590.54330.48170.0373-0.0950.1587-0.11920.7551-0.1666-0.49621.01810.9251-0.4075-1.13320.2979-0.25024.2065-63.7155-225.5239-16.4072
280.47110.02580.08110.0959-0.12340.16140.0555-0.3092-0.36260.1787-0.31110.36220.1806-0.09940.08791.2248-0.4993-0.02331.8693-0.26222.4113-57.5181-231.4469-17.306
290.5335-0.119-0.45760.19440.52940.9828-0.2126-0.0546-0.80990.5602-1.3627-0.16140.48410.4488-1.25860.7947-0.1788-0.70250.52720.08372.6139-46.1264-231.5842-7.5464
300.0908-0.15490.05870.2070.26150.4492-0.00140.7658-0.1660.459-0.90560.445-0.1097-0.4114-0.74011.4551-1.44760.26740.688-2.24694.3789-42.6485-205.372-6.475
310.1368-0.07260.24590.31780.16550.8371-0.41310.1533-0.4012-0.3899-0.1273-0.3247-0.08380.6066-0.11172.2014-0.93651.53032.2789-0.51773.5762-25.2563-176.5809-4.0719
320.7235-0.1995-0.24270.64270.32211.7107-0.40640.3107-0.46090.1345-0.17510.01880.14940.0987-0.79081.04560.01940.72241.45410.39122.1651-6.6728-159.54942.3115
330.35310.02530.07280.25070.29040.3720.5591-0.18440.5034-0.37760.59610.05090.16420.32380.71551.3378-0.4678-0.16290.8883-0.93533.324-36.7046-180.7742-45.1472
340.21340.04160.01040.13650.02380.00820.3751-0.14760.11980.20440.03280.3584-0.33340.11020.08741.44250.0710.27941.0747-2.15082.948-26.5979-167.1884-34.7105
350.0265-0.0099-0.01310.5643-0.14280.0375-0.37870.3046-0.2398-0.2995-0.23220.1855-0.39960.3732-0.1091.46720.8154-0.84970.4744-1.06084.3043-23.8536-183.7498-45.0872
360.3537-0.06140.51730.1620.01270.5777-1.0863-0.15940.7341-0.5098-0.05850.1260.2670.0228-0.55842.3096-0.8150.50211.0306-0.56641.8664-19.1944-181.9343-50.4693
371.5219-0.17450.65580.0422-0.07320.19151.2813-1.09091.72820.33390.5229-0.4353-1.42912.22741.3556-1.96672.3709-2.7611-0.76381.06233.2007-50.4028-225.1654-56.0509
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 40 through 153 )A40 - 153
2X-RAY DIFFRACTION2chain 'A' and (resid 154 through 199 )A154 - 199
3X-RAY DIFFRACTION3chain 'A' and (resid 200 through 386 )A200 - 386
4X-RAY DIFFRACTION4chain 'A' and (resid 387 through 457 )A387 - 457
5X-RAY DIFFRACTION5chain 'B' and (resid 40 through 138 )B40 - 138
6X-RAY DIFFRACTION6chain 'B' and (resid 139 through 251 )B139 - 251
7X-RAY DIFFRACTION7chain 'B' and (resid 252 through 331 )B252 - 331
8X-RAY DIFFRACTION8chain 'B' and (resid 332 through 457 )B332 - 457
9X-RAY DIFFRACTION9chain 'C' and (resid 40 through 85 )C40 - 85
10X-RAY DIFFRACTION10chain 'C' and (resid 86 through 136 )C86 - 136
11X-RAY DIFFRACTION11chain 'C' and (resid 137 through 243 )C137 - 243
12X-RAY DIFFRACTION12chain 'C' and (resid 244 through 303 )C244 - 303
13X-RAY DIFFRACTION13chain 'C' and (resid 304 through 367 )C304 - 367
14X-RAY DIFFRACTION14chain 'C' and (resid 368 through 457 )C368 - 457
15X-RAY DIFFRACTION15chain 'E' and (resid 40 through 136 )E40 - 136
16X-RAY DIFFRACTION16chain 'E' and (resid 137 through 258 )E137 - 258
17X-RAY DIFFRACTION17chain 'E' and (resid 259 through 376 )E259 - 376
18X-RAY DIFFRACTION18chain 'E' and (resid 377 through 457 )E377 - 457
19X-RAY DIFFRACTION19chain 'D' and (resid 40 through 116 )D40 - 116
20X-RAY DIFFRACTION20chain 'D' and (resid 117 through 160 )D117 - 160
21X-RAY DIFFRACTION21chain 'D' and (resid 161 through 376 )D161 - 376
22X-RAY DIFFRACTION22chain 'D' and (resid 377 through 457 )D377 - 457
23X-RAY DIFFRACTION23chain 'F' and (resid 40 through 138 )F40 - 138
24X-RAY DIFFRACTION24chain 'F' and (resid 139 through 163 )F139 - 163
25X-RAY DIFFRACTION25chain 'F' and (resid 164 through 204 )F164 - 204
26X-RAY DIFFRACTION26chain 'F' and (resid 205 through 457 )F205 - 457
27X-RAY DIFFRACTION27chain 'G' and (resid 40 through 116 )G40 - 116
28X-RAY DIFFRACTION28chain 'G' and (resid 117 through 159 )G117 - 159
29X-RAY DIFFRACTION29chain 'G' and (resid 160 through 255 )G160 - 255
30X-RAY DIFFRACTION30chain 'G' and (resid 271 through 367 )G271 - 367
31X-RAY DIFFRACTION31chain 'G' and (resid 368 through 406 )G368 - 406
32X-RAY DIFFRACTION32chain 'G' and (resid 407 through 457 )G407 - 457
33X-RAY DIFFRACTION33chain 'H' and (resid 40 through 85 )H40 - 85
34X-RAY DIFFRACTION34chain 'H' and (resid 86 through 138 )H86 - 138
35X-RAY DIFFRACTION35chain 'H' and (resid 139 through 182 )H139 - 182
36X-RAY DIFFRACTION36chain 'H' and (resid 183 through 279 )H183 - 279
37X-RAY DIFFRACTION37chain 'H' and (resid 280 through 457 )H280 - 457

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more